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Magnesium in PDB 2xau: Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp

Protein crystallography data

The structure of Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp, PDB code: 2xau was solved by H.Walbott, S.Mouffok, R.Capeyrou, S.Lebaron, H.Van Tilbeurgh, Y.Henry, N.Leulliot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.25 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 117.551, 117.551, 254.605, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 22.4

Other elements in 2xau:

The structure of Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp also contains other interesting chemical elements:

Nickel (Ni) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp (pdb code 2xau). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp, PDB code: 2xau:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2xau

Go back to Magnesium Binding Sites List in 2xau
Magnesium binding site 1 out of 2 in the Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1751

b:16.6
occ:1.00
OG1 A:THR123 2.1 13.2 1.0
O A:HOH2750 2.1 18.6 1.0
O A:HOH2747 2.1 14.6 1.0
O A:HOH2290 2.1 15.0 1.0
O3B A:ADP1750 2.1 16.2 1.0
O A:HOH2462 2.2 14.1 1.0
CB A:THR123 3.1 17.0 1.0
PB A:ADP1750 3.3 16.6 1.0
O1B A:ADP1750 3.5 15.1 1.0
O A:SER382 3.8 14.3 1.0
OE2 A:GLU216 3.9 19.3 1.0
OD2 A:ASP215 3.9 14.9 1.0
N A:THR123 4.0 17.7 1.0
O2A A:ADP1750 4.0 19.5 1.0
CG2 A:THR123 4.1 18.1 1.0
CA A:THR123 4.2 16.4 1.0
O2B A:ADP1750 4.3 20.4 1.0
OD1 A:ASP215 4.3 15.4 1.0
O3A A:ADP1750 4.4 14.9 1.0
C A:SER382 4.4 18.4 1.0
CD A:GLU216 4.5 18.9 1.0
CG A:ASP215 4.5 15.6 1.0
O A:THR381 4.5 18.0 1.0
O A:HOH2291 4.5 17.8 1.0
CG A:GLU216 4.6 17.9 1.0
PA A:ADP1750 4.6 18.5 1.0
O A:HOH2465 4.7 15.8 1.0
OE1 A:GLN147 4.7 19.1 1.0
NZ A:LYS122 4.8 18.2 1.0
CA A:SER382 4.8 15.1 1.0
CB A:LYS122 4.9 19.4 1.0
CE A:LYS122 4.9 21.7 1.0
O1A A:ADP1750 5.0 18.7 1.0

Magnesium binding site 2 out of 2 in 2xau

Go back to Magnesium Binding Sites List in 2xau
Magnesium binding site 2 out of 2 in the Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the PRP43P Deah-Box Rna Helicase in Complex with Adp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1749

b:17.3
occ:1.00
O B:HOH2268 2.1 13.7 1.0
OG1 B:THR123 2.1 11.6 1.0
O3B B:ADP1748 2.2 15.7 1.0
O B:HOH2415 2.2 13.9 1.0
O B:HOH2656 2.2 18.1 1.0
O B:HOH2188 2.3 14.7 1.0
CB B:THR123 3.2 15.3 1.0
PB B:ADP1748 3.4 18.1 1.0
O1B B:ADP1748 3.6 18.1 1.0
O B:SER382 3.8 14.0 1.0
OD2 B:ASP215 3.8 14.1 1.0
OE2 B:GLU216 4.0 17.4 1.0
N B:THR123 4.1 17.3 1.0
O2A B:ADP1748 4.1 20.1 1.0
CG2 B:THR123 4.1 14.6 1.0
CA B:THR123 4.2 17.8 1.0
OD1 B:ASP215 4.3 15.2 1.0
CD B:GLU216 4.4 20.1 1.0
O2B B:ADP1748 4.4 18.5 1.0
C B:SER382 4.4 17.2 1.0
O3A B:ADP1748 4.4 15.5 1.0
CG B:ASP215 4.5 17.0 1.0
CG B:GLU216 4.5 19.8 1.0
O B:THR381 4.5 18.3 1.0
O B:HOH2418 4.6 18.3 1.0
O B:HOH2270 4.6 18.3 1.0
PA B:ADP1748 4.7 18.1 1.0
OE1 B:GLN147 4.7 18.6 1.0
NZ B:LYS122 4.9 16.2 1.0
CA B:SER382 4.9 15.4 1.0
CB B:LYS122 4.9 18.7 1.0
CE B:LYS122 5.0 15.9 1.0

Reference:

H.Walbott, S.Mouffok, R.Capeyrou, S.Lebaron, O.Humbert, H.Van Tilbeurgh, Y.Henry, N.Leulliot. PRP43P Contains A Processive Helicase Structural Architecture with A Specific Regulatory Domain. Embo J. V. 29 2194 2010.
ISSN: ISSN 0261-4189
PubMed: 20512115
DOI: 10.1038/EMBOJ.2010.102
Page generated: Wed Aug 14 07:03:08 2024

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